ID   HTPG_ALIFS              Reviewed;         391 AA.
AC   P54650;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Chaperone protein HtpG;
DE   AltName: Full=Heat shock protein HtpG;
DE   AltName: Full=High temperature protein G;
DE   Flags: Fragment;
GN   Name=htpG;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-A1;
RX   PubMed=8188612; DOI=10.1128/jb.176.10.3085-3088.1994;
RA   Katiyar S.K., Edlind T.D.;
RT   "The light organ symbiont Vibrio fischeri possesses a homolog of the Vibrio
RT   cholerae transmembrane transcriptional activator ToxR.";
RL   J. Bacteriol. 176:3085-3088(1994).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; L29053; AAA20501.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54650; -.
DR   SMR; P54650; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..>391
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063020"
FT   NON_TER         391
SQ   SEQUENCE   391 AA;  44516 MW;  716E3121D61C0CE8 CRC64;
     MSEQTANKET RGFQSEVKQL LHLMIHSLYS NKEIFLRELI SNASDASDKL RFKALSNGDL
     YEGNADLGVK LSFNEAANTL TISDNGIGMS REDVIEHLGT IAKSGTADFF SKLSEDQSKD
     SQLIGQFGVG FYSAFIVADA VTVRTRAAGS EKDQGVQWHS EGEGDYTIED ITKESRGTDI
     ILHMREEGKE FLNEWRLKEV IGKYSDHIGI PVSIWAVEKD EEGKDKEGKW EQVNKAQALW
     TRSKSDIEDA EYQEFYKHVS HDFADPLTWS HNKVEGKNDY TSLLYIPAKA PFDMMNRDHK
     SGLKLYVQRV FIMDDAEQFM PTYLRFVKGL IDSNDLPLNV SREILQDNKV TQSLRSACTK
     RVLGMLEKMA KKDDEKYLTF WKQFGQVLKE G